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Literature summary for 1.8.1.9 extracted from

  • Jung, H.-C.; Lim , J.K.; Yang, T.-J.; Kang, S.G.; Lee, H.S.
    Direct electron transfer between the frhAGB-encoded hydrogenase and thioredoxin reductase in the nonmethanogenic archaeon Thermococcus onnurineus NA1 (2020), Appl. Environ. Microbiol., 86, e02630-19 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.8.1.9

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
thioredoxin + NADP+ Thermococcus onnurineus
-
 thioredoxin disulfide + NADPH + H+
-
 r
thioredoxin disulfide + H2 Thermococcus onnurineus
-
 thioredoxin
-
 ?

Organism

Organism UniProt Comment Textmining
Thermococcus onnurineus B6YUA8
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information TrxR from Thermococcus onnurineus strain NA1 is known to catalyze the reduction of disulfide bonds of a Pdo protein by the electrons provided by NAD(P)H Thermococcus onnurineus ?
-
-
thioredoxin + NADP+
-
 Thermococcus onnurineus thioredoxin disulfide + NADPH + H+
-
 r
thioredoxin disulfide + H2
-
 Thermococcus onnurineus thioredoxin
-
 ?

Synonyms

Synonyms Comment Organism
NADP-dependent thioredoxin reductase
-
 Thermococcus onnurineus
NTR
-
 Thermococcus onnurineus
thioredoxin reductase
-
 Thermococcus onnurineus
TON_1603
-
 Thermococcus onnurineus
TrxR
-
 Thermococcus onnurineus

Cofactor

Cofactor Comment Organism Structure
additional information TrxR shows preference for NADPH over NADH Thermococcus onnurineus
NADPH
-
 Thermococcus onnurineus

General Information

General Information Comment Organism
metabolism the TrxR/Pdo redox cascade can use H2 as the electron donor when the frhAGB-encoded hydrogenase mediates electron transfer. When FrhAGB is replaced with FrhAG, it also catalyzes the reduction of Pdo with slightly weaker activity. The specific activity of the FrhAG hydrogenase is 40% lower than that of the FrhAGB hydrogenase Thermococcus onnurineus
physiological function TrxR from the hyperthermophilic archaeon Thermococcus onnurineus strain NA1 is known to catalyze the reduction of disulfide bonds of a Pdo protein by the electrons provided by NAD(P)H. In Thermococcus onnurineus NA1, the frhAGB-encoded hydrogenase, a homologue of the F420-reducing hydrogenase of methanogens, interacts with thioredoxin reductase (TrxR). Electrons derived from H2 oxidation by the frhAGB-encoded hydrogenase are transferred to TrxR and reduced Pdo (protein disulfide oxidoreductase, UniProt ID B6YTB7), a redox partner of TrxR. Interaction and electron transfer are observed between TrxR and the heterodimeric hydrogenase complex (FrhAG) as well as the heterotrimeric complex (FrhAGB). Hydrogen-dependent reduction of TrxR is 7fold less efficient than when NADPH is the electron donor. TrxR can use H2 as an electron donor with the aid of the frhAGB-encoded hydrogenase as well as NADPH in Thermococcus onnurineus strain NA. The frhAGB-encoded hydrogenase can transfer electrons derived from oxidation of H2 to a protein target by direct contact without the involvement of an electron carrier, which is distinct from the mechanism of its homologue, F420-reducing hydrogenases of methanogens. The TrxR (TON_1603) of the hyperthermophilic archaeon Thermococcus onnurineus strain NA1 is a typical prokaryotic NADP-dependent thioredoxin reductase (NTR) with a preference for NADPH over NADH. The TrxR/Pdo redox couple is capable of reducing cystine to cysteine, which subsequently reduced dimethyl sulfoxide (DMSO) to dimethylsulfide (DMS). Because growth is enhanced by substituting DMSO for elemental sulfur (S0) as an electron sink for excess reducing power Thermococcus onnurineus